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  • Title: Phosphorylation of more than one site is required for tight interaction of human tau protein with 14-3-3zeta.
    Author: Sluchanko NN, Seit-Nebi AS, Gusev NB.
    Journal: FEBS Lett; 2009 Sep 03; 583(17):2739-42. PubMed ID: 19647741.
    Abstract:
    Serine residues phosphorylated by protein kinase A (PKA) in the shortest isoform of human tau protein (tau3) were sequentially replaced by alanine and interaction of phosphorylated tau3 and its mutants with 14-3-3 was investigated. Mutation S156A slightly decreased interaction of phosphorylated tau3 with 14-3-3. Double mutations S156A/S267A and especially S156A/S235A, strongly inhibited interaction of phosphorylated tau3 with 14-3-3. Thus, two sites located in the Pro-rich region and in the pseudo repeats of tau3 are involved in phosphorylation-dependent interaction of tau3 with 14-3-3. The state of tau3 phosphorylation affects the mode of 14-3-3 binding and by this means might modify tau filament formation.
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